Evidence map›Paper›PMID 23645667›Full record

ArticleThe Journal of biological chemistry2013

A mechanism for protein monoubiquitination dependent on a trans-acting ubiquitin-binding domain.

Antonio Herrador, Sébastien Léon, Rosine Haguenauer-Tsapis, Olivier Vincent

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 17 papers.

0numbers the graph read from it
0cells of the map it votes in
17citing papers in PubMed
0.9field-weighted citation impact, top 27% of its field
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

17 citing papers in PubMed, 26 citations in OpenAlex.

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  13. Proton Transport and pH Control in Fungi.Advances in experimental medicine and biology · 2016
    Review
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4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

4 authors at 3 institutions in 2 countries.

Antonio HerradorInstituto de Investigaciones Biomédicas, Consejo Superior de Investigaciones Científicas-Universidad Autónoma de Madrid (CSIC-UAM), 28029 Madrid, Spain.
Sébastien LéonInstitut Jacques Monod, Centre National de la Recherche Scientifique, UMR 7592, Université Paris Diderot, Sorbonne Paris Cité, 75205 Paris, France.
Rosine Haguenauer-TsapisInstitut Jacques Monod, Centre National de la Recherche Scientifique, UMR 7592, Université Paris Diderot, Sorbonne Paris Cité, 75205 Paris, France.
Olivier VincentInstituto de Investigaciones Biomédicas, Consejo Superior de Investigaciones Científicas-Universidad Autónoma de Madrid (CSIC-UAM), 28029 Madrid, Spain. Electronic address: ovincent@iib.uam.es.
Universidad Autónoma de Madrid · ESSorbonne Paris Cité · FRUniversité Paris Cité · FR

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The length of the ubiquitin chain on a substrate dictates various functional outcomes, yet little is known about its regulation in vivo. The yeast arrestin-related protein Rim8/Art9 is monoubiquitinated in vivo by the Rsp5 ubiquitin ligase. This also requires Vps23, a protein that displays an ubiquitin-E2 variant (UEV) domain. Here, we report that binding of the UEV domain to Rim8 interferes with ubiquitin chain elongation and directs Rim8 monoubiquitination. We propose that Vps23 UEV competes with Rsp5 HECT N-lobe for binding to the first conjugated ubiquitin, thereby preventing polyubiquitination. These findings reveal a novel mechanism to control ubiquitin chain length on substrates in vivo.

Indexed as

Cell Cycle ProteinsEndosomal Sorting Complexes Required for TransportIntracellular Signaling Peptides and ProteinsProtein Structure, TertiarySaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsUbiquitinUbiquitinationUbiquitin-Protein Ligase ComplexesCell Cycle ProteinsEndosomal Sorting Complexes Required for TransportIntracellular Signaling Peptides and ProteinsRim8 protein, S cerevisiaeRSP5 protein, S cerevisiaeSaccharomyces cerevisiae ProteinsSTP22 protein, S cerevisiaeUbiquitinUbiquitin-Protein Ligase ComplexesArrestinESCRTRsp5UbiquitinUbiquitinationUbiquitin LigaseUbiquitylationUEV

Identifiers

PMID23645667
PMCPMC3675560
OpenAlexW1992254402

What OpenQuestion holds

Textmetadata
Read underepoch 390

Registered trials

None linked

Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.